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Protein

Glutathione S-transferase

Gene

gst

Organism
Ochrobactrum anthropi
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Kineticsi

  1. KM=0.132 mM for glutathione1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei10Glutathione1 Publication1
    Binding sitei35Glutathione1 Publication1
    Binding sitei52Glutathione; via amide nitrogen and carbonyl oxygen1 Publication1

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    BRENDAi2.5.1.18. 4382.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase (EC:2.5.1.18)
    Gene namesi
    Name:gst
    OrganismiOchrobactrum anthropi
    Taxonomic identifieri529 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi10C → A: Strongly reduced affinity for glutathione. Reduces enzyme activity by about 50%. 1 Publication1
    Mutagenesisi11S → A: Reduced activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001859731 – 201Glutathione S-transferaseAdd BLAST201

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi439375.Oant_1298.

    Structurei

    Secondary structure

    1201
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 5Combined sources4
    Helixi12 – 21Combined sources10
    Beta strandi26 – 29Combined sources4
    Turni32 – 35Combined sources4
    Helixi43 – 45Combined sources3
    Beta strandi54 – 58Combined sources5
    Beta strandi61 – 65Combined sources5
    Helixi66 – 75Combined sources10
    Helixi80 – 82Combined sources3
    Helixi89 – 109Combined sources21
    Helixi110 – 112Combined sources3
    Helixi118 – 138Combined sources21
    Beta strandi148 – 150Combined sources3
    Helixi153 – 167Combined sources15
    Helixi176 – 186Combined sources11
    Helixi189 – 197Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2NTOX-ray2.10A1-201[»]
    2PVQX-ray1.80A1-201[»]
    ProteinModelPortaliP81065.
    SMRiP81065.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81065.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini1 – 81GST N-terminalAdd BLAST81
    Domaini87 – 201GST C-terminalAdd BLAST115

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni65 – 66Glutathione binding1 Publication2
    Regioni102 – 105Glutathione binding1 Publication4

    Sequence similaritiesi

    Belongs to the GST superfamily. Beta family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiENOG4108K3A. Bacteria.
    COG0625. LUCA.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF14497. GST_C_3. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P81065-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKLYYKVGAC SLAPHIILSE AGLPYELEAV DLKAKKTADG GDYFAVNPRG
    60 70 80 90 100
    AVPALEVKPG TVITQNAAIL QYIGDHSDVA AFKPAYGSIE RARLQEALGF
    110 120 130 140 150
    CSDLHAAFSG LFAPNLSEEA RAGVIANINR RLGQLEAMLS DKNAYWLGDD
    160 170 180 190 200
    FTQPDAYASV IIGWGVGQKL DLSAYPKALK LRERVLARPN VQKAFKEEGL

    N
    Length:201
    Mass (Da):21,739
    Last modified:May 30, 2000 - v2
    Checksum:i763B2D3DECA21F2D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y17279 Genomic DNA. Translation: CAA76728.1.
    RefSeqiWP_010659377.1. NZ_KK073936.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y17279 Genomic DNA. Translation: CAA76728.1.
    RefSeqiWP_010659377.1. NZ_KK073936.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2NTOX-ray2.10A1-201[»]
    2PVQX-ray1.80A1-201[»]
    ProteinModelPortaliP81065.
    SMRiP81065.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi439375.Oant_1298.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiENOG4108K3A. Bacteria.
    COG0625. LUCA.

    Enzyme and pathway databases

    BRENDAi2.5.1.18. 4382.

    Miscellaneous databases

    EvolutionaryTraceiP81065.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF14497. GST_C_3. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGST_OCHAN
    AccessioniPrimary (citable) accession number: P81065
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 30, 2000
    Last modified: November 2, 2016
    This is version 80 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.